5D3O

Crystal structure of full length human glutaminase C expressed in E.coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004359	molecular_function	glutaminase activity
A	0006541	biological_process	glutamine metabolic process
B	0004359	molecular_function	glutaminase activity
B	0006541	biological_process	glutamine metabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1

Chain	Residue	Details
A	SER291
B	TYR419
B	TYR471
B	VAL489
A	ASN340
A	GLU386
A	TYR419
A	TYR471
A	VAL489
B	SER291
B	ASN340
B	GLU386

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP1

Chain	Residue	Details
A	ASN393
B	ASN393

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Cleavage; by MPP => ECO:0000250|UniProtKB:P13264

Chain	Residue	Details
A	LEU77
B	LEU77

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:D3Z7P3

Chain	Residue	Details
A	LYS135
A	LYS169
B	LYS135
B	LYS169

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS316
B	LYS316

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